Crystal structure of the nuclear matrix targeting signal of the transcription factor acute myelogenous leukemia-1/polyoma enhancer-binding protein 2αB/core binding factor α2

Academic Article

Abstract

  • Transcription factors of the acute myelogenous leukemia (AML)/polyoma enhancer-binding protein (PEBP2α)/core-binding factor α (CBFA) class are key transactivators of tissue-specific genes of the hematopoietic and bone lineages. AML-1/PEBP2αB/CBFA2 proteins participating in transcription are associated with the nuclear matrix. This association is solely dependent on a highly conserved C-terminal protein segment, designated the nuclear matrix targeting signal (NMTS). The NMTS of AML-1 is physically distinct from the nuclear localization signal, operates autonomously, and supports transactivation. Our data indicate that the related AML-3 and AML-2 proteins are also targeted to the nuclear matrix in situ by analogous C-terminal domains. Here we report the first crystal structure of an NMTS in an AML-1 segment fused to glutathione S-transferase. The model of the NMTS consists of two loops connected by a flexible U-shaped peptide chain.
  • Published In

    Digital Object Identifier (doi)

    Author List

  • Tang L; Guo B; Javed A; Choi JY; Hiebert S; Lian JB; Van Wijnen AJ; Stein JL; Stein GS; Zhou GW
  • Start Page

  • 33580
  • End Page

  • 33586
  • Volume

  • 274
  • Issue

  • 47